SCP26_ARATH
ID SCP26_ARATH Reviewed; 452 AA.
AC Q9ZQQ0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine carboxypeptidase-like 26;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL26; OrderedLocusNames=At2g35780; ORFNames=T20F21.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15908604; DOI=10.1104/pp.104.057950;
RA Fraser C.M., Rider L.W., Chapple C.;
RT "An expression and bioinformatics analysis of the Arabidopsis serine
RT carboxypeptidase-like gene family.";
RL Plant Physiol. 138:1136-1148(2005).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC006068; AAM15111.1; -; Genomic_DNA.
DR EMBL; AC007017; AAD21479.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09160.1; -; Genomic_DNA.
DR EMBL; AY088044; AAM65590.1; -; mRNA.
DR EMBL; BT029178; ABJ17113.1; -; mRNA.
DR PIR; H84772; H84772.
DR RefSeq; NP_181121.1; NM_129136.5.
DR AlphaFoldDB; Q9ZQQ0; -.
DR SMR; Q9ZQQ0; -.
DR STRING; 3702.AT2G35780.1; -.
DR ESTHER; arath-SCP26; Carboxypeptidase_S10.
DR MEROPS; S10.A43; -.
DR PaxDb; Q9ZQQ0; -.
DR PRIDE; Q9ZQQ0; -.
DR ProteomicsDB; 232939; -.
DR EnsemblPlants; AT2G35780.1; AT2G35780.1; AT2G35780.
DR GeneID; 818150; -.
DR Gramene; AT2G35780.1; AT2G35780.1; AT2G35780.
DR KEGG; ath:AT2G35780; -.
DR Araport; AT2G35780; -.
DR TAIR; locus:2039275; AT2G35780.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; Q9ZQQ0; -.
DR OMA; YTVTCKK; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9ZQQ0; -.
DR PRO; PR:Q9ZQQ0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQQ0; baseline and differential.
DR Genevisible; Q9ZQQ0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..452
FT /note="Serine carboxypeptidase-like 26"
FT /id="PRO_0000274641"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT ACT_SITE 375
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..338
FT /evidence="ECO:0000250"
FT DISULFID 244..256
FT /evidence="ECO:0000250"
FT DISULFID 280..306
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 51521 MW; BA25B878273C470F CRC64;
MARLLLLFFF FLILLHYASC SRHEQEKDRI FHLPGEPNDV SFSHFSGYIT VNESAGRALF
YWLTESPPSE NPESKPLVLW LNGGPGCSSV AYGAAEEIGP FRINPDGKTL YHNPYSWNKL
ANLLFLESPA GVGFSYSNTT SDLYTAGDQR TAEDAYVFLV KWFERFPQYK HREFYIAGES
YAGHYVPQLS QIVYEKRNPA INFKGFIVGN AVIDDYHDYV GLFEYWWAHG LISDLTYHNL
RITCEFGSSE HPSSKCTKAM EAADLEQGNI DPYSIYTVTC KKEAAALRSR FSRVRHPWMW
RAYDPCTEKY SGMYFNSPEV QKAMHANITG LAYPWKGCSD IVGEKWADSP LSMLPIYKEL
IAAGLRIWVF SGDTDSVVPI TGTRYSIRAL KLQPLSKWYP WNDDGQVGGW SQVYKGLTLV
TIHGAGHEVP LFRPRRAFLL FQSFLDNKPL PM